Binding Induced Intrinsically Disordered Protein Folding with Molecular Dynamics Simulation

摘要: Intrinsically disordered proteins lack stable tertiary and/or secondary structures under physiological conditions in vitro. undergo significant conformational transitions to well folded forms only on binding partner. Molecular dynamics simulations are used research the mechanism of folding for intrinsically protein upon partner binding. Room-temperature MD suggest that have nonspecific and specific interactions with Kinetic analysis high-temperature shows bound apo-states unfold via a two-state process, respectively. Φ-value can identify key residues proteins. Kolmogorov-Smirnov (KS) P test illustrates recognition between might follow induced-fit mechanism. Furthermore, these methods be widely induced